ID D5C0K5_NITHN Unreviewed; 438 AA.
AC D5C0K5;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Amino-acid acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01105};
DE EC=2.3.1.1 {ECO:0000256|HAMAP-Rule:MF_01105};
DE AltName: Full=N-acetylglutamate synthase {ECO:0000256|HAMAP-Rule:MF_01105};
DE Short=AGS {ECO:0000256|HAMAP-Rule:MF_01105};
DE Short=NAGS {ECO:0000256|HAMAP-Rule:MF_01105};
GN Name=argA {ECO:0000256|HAMAP-Rule:MF_01105};
GN OrderedLocusNames=Nhal_3281 {ECO:0000313|EMBL:ADE16328.1};
OS Nitrosococcus halophilus (strain Nc4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Nitrosococcus.
OX NCBI_TaxID=472759 {ECO:0000313|EMBL:ADE16328.1, ECO:0000313|Proteomes:UP000001844};
RN [1] {ECO:0000313|Proteomes:UP000001844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nc4 {ECO:0000313|Proteomes:UP000001844};
RG US DOE Joint Genome Institute;
RA Campbell M.A., Malfatti S.A., Chain P.S.G., Heidelberg J.F., Ward B.B.,
RA Klotz M.G.;
RT "Complete genome sequence of Nitrosococcus halophilus Nc4, a salt-adapted,
RT aerobic obligate ammonia-oxidizing sulfur purple bacterium.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate;
CC Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000016, ECO:0000256|HAMAP-
CC Rule:MF_01105};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 1/4. {ECO:0000256|ARBA:ARBA00004925,
CC ECO:0000256|HAMAP-Rule:MF_01105}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01105}.
CC -!- MISCELLANEOUS: In bacteria which possess the bifunctional enzyme
CC ornithine acetyltransferase/N-acetylglutamate synthase (ArgJ), ArgA
CC fulfills an anaplerotic role. {ECO:0000256|HAMAP-Rule:MF_01105}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily.
CC {ECO:0000256|ARBA:ARBA00009145, ECO:0000256|HAMAP-Rule:MF_01105}.
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DR EMBL; CP001798; ADE16328.1; -; Genomic_DNA.
DR RefSeq; WP_013034177.1; NC_013960.1.
DR AlphaFoldDB; D5C0K5; -.
DR STRING; 472759.Nhal_3281; -.
DR KEGG; nhl:Nhal_3281; -.
DR eggNOG; COG0548; Bacteria.
DR eggNOG; COG1246; Bacteria.
DR HOGENOM; CLU_024773_0_0_6; -.
DR OrthoDB; 9802238at2; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000001844; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd04237; AAK_NAGS-ABP; 1.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR HAMAP; MF_01105; N_acetyl_glu_synth; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR033719; NAGS_kin.
DR InterPro; IPR010167; NH2A_AcTrfase.
DR NCBIfam; TIGR01890; N-Ac-Glu-synth; 1.
DR PANTHER; PTHR30602; AMINO-ACID ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR30602:SF12; AMINO-ACID ACETYLTRANSFERASE NAGS1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR PIRSF; PIRSF000423; ArgA; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_01105};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01105};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_01105}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01105};
KW Reference proteome {ECO:0000313|Proteomes:UP000001844};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01105}.
FT DOMAIN 292..431
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 438 AA; 47984 MW; 09C39B25F935720C CRC64;
MSTDHPLPEA HWFRNAAPYI HAHRGRTFVI AFTGEAIQGP TFPHLIHDIA LLGSLGIQLV
LVHGARPQIE ATLAQRGLNL RYVNGLRVTD DAALFCVKQA IGAVRVEIEA LLSMGLPNSP
MAGAQVRVAA GNFITARPLG VREGVDYCHT GEVRKVDIEA IRQRLNSGAI VLLSPLGYSL
TGEVFNLSAE EVATVSAIAL GADKLIFIGT GLPAAAPSPL PRELNPQEAE QLLRSTSELP
DELVCHLQSA IHACRSRVPR VHIIDQHLDG ALLMELFSRD GIGTLVTAIA FEDTRRAMIE
DVGGILELIA PLEERGLLVR RSRERLEMEI HHFTVMERDG TIIGCAALYP FPEEKIGELA
CLVVHPDYRQ SGRATALLTG IEKAAKQQGL SRLCVLTTQT AHWFRERGFE PSSLEALPEN
KRALYNYQRN SKVFVKSL
//
